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. 2016 Sep 1;22(6):446–460. doi: 10.1089/mdr.2016.0050

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© Robert M. Cleverley et al., 2016; Published by Mary Ann Liebert, Inc.

This Open Access article is distributed under the terms of the Creative Commons Attribution Noncommercial License (http://creativecommons.org/licenses/by-nc/4.0/) which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited.

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FIG. 8. — GpsB does not affect the enzyme activities of PBP1 in vitro. (A) The GTase activity of BsPBP1 in the presence (blue line) and absence of wild-type BsGpsB (red line), BsGpsB_T75D (green line), and BsGpsB_T75E (magenta line) was measured using fluorescently labeled lipid II as described previously.⁴⁰ In the absence of BsPBP1 (black line), no lipid II consumption is observed. Each measurement is shown as the mean ± SD (n = 3). (B) HPLC chromatograms from in vitro PG synthesis assays. BsPBP1 in the presence and absence of BsGpsB was incubated with radiolabeled amidated lipid II-m-DAP. The resultant PG was digested, boiled, and reduced before the resulting muropeptides were separated by HPLC. Peak 1—disaccharide pentapeptide(NH₂) monophosphate resulting from unused substrate and glycan chain ends; peak 2—disaccharide tetrapeptide(NH₂) derived from GTase and carboxypeptidase activity; peak 3—disaccharide pentapeptide (nonamidated) from the GTase activity on contaminating nonamidated substrate; peak 4—disaccharide pentapeptide(NH₂) resulting from the GTase activity; peak 5—bis-disaccharide tetrapeptide(2NH₂) resulting from GTase, TPase, and carboxypeptidase activities; peak 6—bis-disaccharide tetrapentapeptide(2NH₂) resulting from GTase and TPase activities. HPLC, high-pressure liquid chromatography.